ID A0A5B6WMS9_9ROSI Unreviewed; 601 AA.
AC A0A5B6WMS9;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=EPI10_004447 {ECO:0000313|EMBL:KAA3482182.1};
OS Gossypium australe.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=47621 {ECO:0000313|EMBL:KAA3482182.1, ECO:0000313|Proteomes:UP000325315};
RN [1] {ECO:0000313|Proteomes:UP000325315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. PA1801 {ECO:0000313|Proteomes:UP000325315};
RX PubMed=31479566; DOI=10.1111/pbi.13249;
RA Cai Y., Cai X., Wang Q., Wang P., Zhang Y., Cai C., Xu Y., Wang K.,
RA Zhou Z., Wang C., Geng S., Li B., Dong Q., Hou Y., Wang H., Ai P., Liu Z.,
RA Yi F., Sun M., An G., Cheng J., Zhang Y., Shi Q., Xie Y., Shi X., Chang Y.,
RA Huang F., Chen Y., Hong S., Mi L., Sun Q., Zhang L., Zhou B., Peng R.,
RA Zhang X., Liu F.;
RT "Genome sequencing of the Australian wild diploid species Gossypium
RT australe highlights disease resistance and delayed gland morphogenesis.";
RL Plant Biotechnol. J. 0:0-0(2019).
CC -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3
CC complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating
CC enzymes and then transfers it to substrates.
CC {ECO:0000256|ARBA:ARBA00003976}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAA3482182.1}.
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DR EMBL; SMMG02000002; KAA3482182.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B6WMS9; -.
DR OrthoDB; 10009520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000325315; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR CDD; cd22586; Rcat_RBR_ARI1-like; 1.
DR CDD; cd16773; RING-HC_RBR_TRIAD1; 1.
DR FunFam; 1.20.120.1750:FF:000013; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR048962; ARIH1-like_UBL.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR054694; Parkin-like_IBR.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22605; IBR_2; 1.
DR Pfam; PF21235; UBA_ARI1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000325315};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 129..343
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 133..181
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..11
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 601 AA; 69169 MW; 13F95879788D6CE5 CRC64;
MEDFSSSDED YYYSSDRDSL DGFQNDESDS QWVTSKSPTT KLRRTNLAFI QVITKESLLA
AQREDLRRVM DMLSIREHHA RTLLIHYRWD VEKLLAVLVE NGKSYLFASA GVSVVEGEHT
GTSVLSLSST SMCEICIEEL PVDKMTKMEC GHGFCNDCWT EHFVVKINDG QSRRIRCMAH
KCNAVCDESV VRNLVSKRHP DLAKKFDRFL LESYIEDNRM VKWCPSTPHC GNAIRVEDDE
FCEVECSCGL QFCFSCLSEA HSPCSCMMWE LWTKKCRDES ETVNWITVHT KPCPQCHKPV
EKNGGCNLVS CICGQAFCWL CGGATGRDHT WSTIAGHSCG RYKEDQAKKT ERAKRDLYRY
MHYLNRYKAH TDSFKLESKL KETILEKISI SEERESILRD FSWVTNGLNR LFRSRRVLSY
SYPFAFYMFG EEIFVDEMTN KEREIKQHLF EDQQQQLEAN VEKLSKILEE PFDQYSDDKV
TEMRMQIINL TVITDTLCKK MYECIENDLL GSLQCNTHNI APYKSKGIEK ASELAVCWNS
KPSTTEKCVT SDSGTSGKRD RPFGFGSSED SGCPSHRRPK KETYGGVFFD ISMPAEVLHR
N
//
